ID A0A1Z4R321_9CYAN Unreviewed; 312 AA.
AC A0A1Z4R321;
DT 27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Peptidase U61 LD-carboxypeptidase A {ECO:0000313|EMBL:BAZ36845.1};
GN ORFNames=NIES4101_27650 {ECO:0000313|EMBL:BAZ36845.1};
OS Calothrix sp. NIES-4101.
OG Plasmid Plasmid5 dna {ECO:0000313|Proteomes:UP000290974}.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Calotrichaceae;
OC Calothrix.
OX NCBI_TaxID=2005461 {ECO:0000313|EMBL:BAZ36845.1, ECO:0000313|Proteomes:UP000290974};
RN [1] {ECO:0000313|EMBL:BAZ36845.1, ECO:0000313|Proteomes:UP000290974}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIES-4101 {ECO:0000313|EMBL:BAZ36845.1,
RC ECO:0000313|Proteomes:UP000290974};
RC PLASMID=Plasmid5 dna {ECO:0000313|Proteomes:UP000290974};
RA Hirose Y., Shimura Y., Fujisawa T., Nakamura Y., Kawachi M.;
RT "Genome sequencing of cyanobaciteial culture collection at National
RT Institute for Environmental Studies (NIES).";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; AP018278; BAZ36845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z4R321; -.
DR Proteomes; UP000290974; Plasmid Plasmid5 dna.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07025; Peptidase_S66; 1.
DR Gene3D; 3.40.50.10740; Class I glutamine amidotransferase-like; 1.
DR Gene3D; 3.50.30.60; LD-carboxypeptidase A C-terminal domain-like; 1.
DR InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR027478; LdcA_N.
DR InterPro; IPR040449; Peptidase_S66_N.
DR InterPro; IPR040921; Peptidase_S66C.
DR InterPro; IPR003507; S66_fam.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30237:SF2; MUREIN TETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR Pfam; PF02016; Peptidase_S66; 1.
DR Pfam; PF17676; Peptidase_S66C; 1.
DR PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF141986; LD-carboxypeptidase A C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:BAZ36845.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Plasmid {ECO:0000313|EMBL:BAZ36845.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000290974};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 15..134
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 183..297
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 214
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 282
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 312 AA; 34199 MW; EFCB23112C347E4A CRC64;
MKIVHPPRLS HGDLIGVVSG SAPETLLEPT WFQRGLDVLK AKGYQTALSA QLQKRNGYLS
GSETAMAQDL LGFLHDPMVK AVLFAGGGTN ANRMLRHLDL KGFSDYPKII IGLSNPSTLL
NAVHTKTGVV TFHGPALIWN MGNPNGLTNY TSKHFWSLIE SPTESFIYEP TPSWFWLKEG
KASGRLLGGN LISIQTLLGT SWEPSFDDSI FFWEDISKPI NRLDLMLTHF RDAGVFDRIS
GMVVGNLVNC DPPEGGQTLS EMLLEITDGY SFPILTGVSL GHTDDKITLP IGIRASLDSI
NNTFQLLESA VR
//
